Structure of PDB 1orr Chain D

Receptor sequence

>1orrD (length=336)

AKLLITGGCGFLGSNLASFALSQGIDLIVFDNLSRKGATDNLHWLSSLGN
FEFVHGDIRNKNDVTRLITKYMPDSCFHLAGQVAMTTSIDNPCMDFEINV
GGTLNLLEAVRQYNSNCNIIYSSTNKVYGDLEQYKYNETETRYTCVDKPN
GYDESTQLDFHSPYGCSKGAADQYMLDYARIFGLNTVVFRHSSMYGGRQF
ATYDQGWVGWFCQKAVEIKNGIPFTISGNGKQVRDVLHAEDMISLYFTAL
ANVSKIRGNAFNIGGTIVNSLSLLELFKLLEDYCNIDMRFTNLPVRESDQ
RVFVADIKKITNAIDWSPKVSAKDGVQKMYDWTSSI

3D structure

• PDB: 1orr High Resolution X-ray Structure of Tyvelose Epimerase from Salmonella typhi
• Chain: D
• Resolution: 1.5 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): T125 N126 K127 Y165 K169
• Catalytic site (residue number reindexed from 1): T124 N125 K126 Y164 K168
• Enzyme Commision number: 5.1.3.10: CDP-paratose 2-epimerase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	NAD	D	G8 G11 F12 L13 D32 N33 S35 R36 D58 I59 L80 V84 S123 S124 K169 H192 M195 Q206	G7 G10 F11 L12 D31 N32 S34 R35 D57 I58 L79 V83 S122 S123 K168 H191 M194 Q205
BS02	CDP	D	Y204 W208 W211 F212 S230 Q235 R237 L276 R299 D302	Y203 W207 W210 F211 S227 Q232 R234 L273 R296 D299

Gene Ontology

Molecular Function

• GO:0008460 dTDP-glucose 4,6-dehydratase activity
• GO:0016853 isomerase activity
• GO:0047732 CDP-abequose epimerase activity

Biological Process

• GO:0009103 lipopolysaccharide biosynthetic process

External links

• PDB: RCSB:1orr, PDBe:1orr, PDBj:1orr
• PDBsum: 1orr
• PubMed: 12642575
• UniProt: P14169|RFBE_SALTI CDP-paratose 2-epimerase (Gene Name=rfbE)